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Literature summary extracted from

  • Shang, F.; Chen, J.; Wang, L.; Jin, L.; Zou, L.; Bu, T.; Dong, Y.; Ha, N.C.; Nam, K.H.; Quan, C.; Xu, Y.
    Crystal structure of the nicotinamidase/pyrazinamidase PncA from Bacillus subtilis (2018), Biochem. Biophys. Res. Commun., 503, 2906-2911 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.B15 determination and analysis of the crystal structure of substrate-free PncA from Bacillus subtilis (BsPncA) at 2.0 A resolution Bacillus subtilis
3.5.1.19 sitting-drop vapor-diffusion method at 14°C. The crystal structure is determined at 2.0 A resolution. The structure of BsPncA consists of an alpha/beta domain and a subdomain. The subdomain of BsPncA has a different conformation than that of PncA enzymes from other organisms. The B-factor analysis revealed a rigid structure of the alpha/beta domain, while the subdomain is highly flexible. Both dimers and tetramers are observed in crystals, but only dimers are observed in solution Bacillus velezensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.B15 pyrazinamide + H2O Bacillus subtilis
-
 pyrazinoic acid + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.B15 Bacillus subtilis
-
-
-
3.5.1.19 Bacillus velezensis A0A223CGG0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.B15 pyrazinamide + H2O
-
 Bacillus subtilis pyrazinoic acid + NH3
-
 ?
3.5.1.19 nicotinamide + H2O
-
 Bacillus velezensis nicotinate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.B15 dimer or tetramer the structure of BsPncA consists of an alpha/beta domain and a subdomain. The subdomain of BsPncA has a different conformation compared to PncA enzymes from other organisms. The B-factor analysis reveals a rigid structure of the alpha/beta domain, while the subdomain is highly flexible. Both dimers and tetramers are observed in BsPncA protein crystals, but only dimers are observed in solution Bacillus subtilis
3.5.1.19 dimer both dimers and tetramers are observed in crystals, but only dimers are observed in solution Bacillus velezensis
3.5.1.19 tetramer both dimers and tetramers are observed in crystals, but only dimers are observed in solution Bacillus velezensis

Synonyms

EC Number Synonyms Comment Organism
3.5.1.B15 BsPncA
-
 Bacillus subtilis
3.5.1.B15 More cf. EC 3.5.1.19 Bacillus subtilis
3.5.1.B15 nicotinamidase/pyrazinamidase
-
 Bacillus subtilis
3.5.1.B15 PncA
-
 Bacillus subtilis
3.5.1.19 nicotinamidase/pyrazinamidase PncA
-
 Bacillus velezensis

General Information

EC Number General Information Comment Organism
3.5.1.B15 evolution the nicotinamidase/pyrazinamidase PncA is a member of a large family of hydrolase enzymes that catalyze the deamination of nicotinamide to nicotinic acid Bacillus subtilis
3.5.1.B15 physiological function nicotinamidase/pyrazinamidase PncA catalyzes the deamination of nicotinamide to nicotinic acid (EC 3.5.1.19). PncA also functions as a pyrazinamidase in a wide variety of eubacteria and is an essential coenzyme in many cellular redox reactions in living systems Bacillus subtilis